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      Creatinine Inhibits D-Amino Acid Oxidase


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          Inhibition of D-amino acid oxidase (DAO) activity by various uremic retention products and guanidino compounds was investigated. Creatinine (CTN) was found to inhibit DAO at a similar concentration in the sera of uremic patients. The inhibition was competitive and the K<sub>i</sub> value was 2.7 m M. Moreover, CTN was shown to interact with flavin adenine dinucleotide (FAD), a coenzyme of DAO. The UV spectral change of FAD bound to DAO was observed in the visible region by addition of CTN. These findings suggest that the increase in serum and tissue CTN concentrations might be responsible, in part, for the increase in D-amino acids in the sera of uremic patients.

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          Most cited references5

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          Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission.

          Although D amino acids are prominent in bacteria, they generally are thought not to occur in mammals. Recently, high levels of D-serine have been found in mammalian brain where it activates glutamate/N-methyl-D-aspartate receptors by interacting with the "glycine site" of the receptor. Because amino acid racemases are thought to be restricted to bacteria and insects, the origin of D-serine in mammals has been puzzling. We now report cloning and expression of serine racemase, an enzyme catalyzing the formation of D-serine from L-serine. Serine racemase is a protein representing an additional family of pyridoxal-5' phosphate-dependent enzymes in eukaryotes. The enzyme is enriched in rat brain where it occurs in glial cells that possess high levels of D-serine in vivo. Occurrence of serine racemase in the brain demonstrates the conservation of D-amino acid metabolism in mammals with implications for the regulation of N-methyl-D-aspartate neurotransmission through glia-neuronal interactions.
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            o-Phthalaldehyde—N-acetyl-L-cysteine as a chiral derivatization reagent for liquid chromatographic optical resolution of amino acid ernantiomers and its application to conventional amino acid analysis

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              Exaggerated responses to chronic nociceptive stimuli and enhancement of N-methyl-D-aspartate receptor-mediated synaptic transmission in mutant mice lacking D-amino-acid oxidase.

              Formalin-induced nociceptive behaviors and N-methyl-D-aspartate (NMDA) subtype glutamate receptor-mediated excitatory synaptic transmission were analyzed in mutant mice lacking D-amino-acid oxidase, which catalyzes the oxidative deamination of D-amino acids. The second phase of the formalin-induced licking response, a part of which is known to be mediated by NMDA receptors in the spinal cord, was significantly augmented in mutant mice. NMDA receptor-mediated excitatory postsynaptic currents recorded from spinal cord dorsal horn neurons by tight-seal whole-cell methods were significantly potentiated in mutant mice. The present observations provide another line of evidence that D-serine functions as an endogenous coagonist at the glycine site of NMDA receptors, and raise the possibility that D-amino-acid oxidase exerts a neuromodulatory function by controlling the concentration of D-serine in the central nervous system.

                Author and article information

                S. Karger AG
                June 2002
                03 June 2002
                : 91
                : 2
                : 281-285
                aFaculty of Pharmaceutical Sciences, Teikyo University, Sagamiko, Kanagawa; bSchool of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan
                58405 Nephron 2002;91:281–285
                © 2002 S. Karger AG, Basel

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                Page count
                Figures: 3, Tables: 2, References: 34, Pages: 5
                Self URI (application/pdf): https://www.karger.com/Article/Pdf/58405
                Self URI (text/html): https://www.karger.com/Article/FullText/58405
                Self URI (journal page): https://www.karger.com/SubjectArea/Nephrology
                Original Paper

                Cardiovascular Medicine,Nephrology
                Creatinine,Uremia,Inhibition,<italic>D</italic>-Amino acid oxidase,<italic>D</italic>-Amino acid


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